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Database: UniProt
Entry: A0A0A1H3J2_9BURK
LinkDB: A0A0A1H3J2_9BURK
Original site: A0A0A1H3J2_9BURK 
ID   A0A0A1H3J2_9BURK        Unreviewed;       596 AA.
AC   A0A0A1H3J2;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   RecName: Full=Acetolactate synthase {ECO:0000256|ARBA:ARBA00013145, ECO:0000256|RuleBase:RU003591};
DE            EC=2.2.1.6 {ECO:0000256|ARBA:ARBA00013145, ECO:0000256|RuleBase:RU003591};
GN   ORFNames=E1O_07130 {ECO:0000313|EMBL:BAP87844.1};
OS   Burkholderiales bacterium GJ-E10.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales.
OX   NCBI_TaxID=1469502 {ECO:0000313|EMBL:BAP87844.1, ECO:0000313|Proteomes:UP000031649};
RN   [1] {ECO:0000313|EMBL:BAP87844.1, ECO:0000313|Proteomes:UP000031649}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GJ-E10 {ECO:0000313|EMBL:BAP87844.1,
RC   ECO:0000313|Proteomes:UP000031649};
RA   Fukushima J., Tojo F., Asano R., Kobayashi Y., Shimura Y., Okano K.,
RA   Miyata N.;
RT   "Complete Genome Sequence of the Unclassified Iron-Oxidizing,
RT   Chemolithoautotrophic Burkholderiales bacterium GJ-E10 Isolated from Acid
RT   River.";
RL   Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + 2 pyruvate = (2S)-2-acetolactate + CO2;
CC         Xref=Rhea:RHEA:25249, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:58476; EC=2.2.1.6;
CC         Evidence={ECO:0000256|ARBA:ARBA00000673,
CC         ECO:0000256|RuleBase:RU003591};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|RuleBase:RU003591};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|RuleBase:RU003591};
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|RuleBase:RU003591};
CC       Note=Binds 1 thiamine pyrophosphate per subunit.
CC       {ECO:0000256|RuleBase:RU003591};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-
CC       isoleucine from 2-oxobutanoate: step 1/4.
CC       {ECO:0000256|ARBA:ARBA00004974, ECO:0000256|RuleBase:RU003591}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from
CC       pyruvate: step 1/4. {ECO:0000256|ARBA:ARBA00005025,
CC       ECO:0000256|RuleBase:RU003591}.
CC   -!- SIMILARITY: Belongs to the TPP enzyme family.
CC       {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU003591}.
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DR   EMBL; AP014683; BAP87844.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0A1H3J2; -.
DR   STRING; 1469502.E1O_07130; -.
DR   KEGG; bbag:E1O_07130; -.
DR   HOGENOM; CLU_013748_1_3_4; -.
DR   OrthoDB; 2254214at2; -.
DR   UniPathway; UPA00047; UER00055.
DR   UniPathway; UPA00049; UER00059.
DR   Proteomes; UP000031649; Chromosome.
DR   GO; GO:0003984; F:acetolactate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0009099; P:valine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd02015; TPP_AHAS; 1.
DR   CDD; cd07035; TPP_PYR_POX_like; 1.
DR   Gene3D; 3.40.50.970; -; 2.
DR   Gene3D; 3.40.50.1220; TPP-binding domain; 1.
DR   InterPro; IPR012846; Acetolactate_synth_lsu.
DR   InterPro; IPR039368; AHAS_TPP.
DR   InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR012000; Thiamin_PyroP_enz_cen_dom.
DR   InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR   InterPro; IPR045229; TPP_enz.
DR   InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR   NCBIfam; TIGR00118; acolac_lg; 1.
DR   PANTHER; PTHR18968:SF13; ACETOLACTATE SYNTHASE, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR18968; THIAMINE PYROPHOSPHATE ENZYMES; 1.
DR   Pfam; PF02775; TPP_enzyme_C; 1.
DR   Pfam; PF00205; TPP_enzyme_M; 1.
DR   Pfam; PF02776; TPP_enzyme_N; 1.
DR   SUPFAM; SSF52467; DHS-like NAD/FAD-binding domain; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605,
KW   ECO:0000256|RuleBase:RU003591};
KW   Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304,
KW   ECO:0000256|RuleBase:RU003591}; FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Magnesium {ECO:0000256|RuleBase:RU003591};
KW   Metal-binding {ECO:0000256|RuleBase:RU003591};
KW   Reference proteome {ECO:0000313|Proteomes:UP000031649};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU003591};
KW   Transferase {ECO:0000256|RuleBase:RU003591}.
FT   DOMAIN          32..147
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          221..356
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          418..567
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   596 AA;  65162 MW;  7B43E6A5B8987121 CRC64;
     MRSVVPESAP AASLSPATAA AAVPSPETDL LTGAEILVRC LREEGVRHVF GYPGGAVLYI
     YDAIFKQDSF QHILVRHEQA AVHAADAYSR SSRKVGVAIV TSGPGATNAV TGIATAYMDS
     IPLVIISGQV PTHAIGQDAF QECDTVGITR PCVKHNFLVK NVADLAPTIR KAFHIAQTGR
     PGPVLVDVPK DITIARHAFS YPRDLHLRSY NPVVKGHMGQ IKKAVQLLLA AERPLIYTGG
     GVILANATEE LGRLVDRLGF PCTSTLMGLG GYPASDKKFL GMLGMHGTIE ANFAMQHCDV
     LLAVGARFDD RVIGSPAHFA QNPRKIIHID IDPSSISKRV KVDVPIVGDV REVLAEILAQ
     VDAAGGRAAA IDAWWDQLGT WRSQDCLRYE RSETVVKPQH VVETLWNLTG GDIFVTSDVG
     QHQMWAAQYY RFDKPRRWIN SGGLGTMGVG LPYAMGVQMA NPGAQVAVIT GEGSIQMNIQ
     ELSTCRQYRL TPKIINLNNR YLGMVRQWQQ IEYGSRYSES YMDALPDFVR LAEAYGHVGM
     RIDKPADVEP ALREAFTTYR DRLVFLDFIT DSSENVWPMV RAGKGLTEMM LGAEEL
//
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